128718-95-6Relevant articles and documents
Novel Inhibitors of Human Renin Unrelated to the Angiotensinogen sequence. Analogues of a tetrapeptide, Boc-D-Cys(Acm)-D-Trp-Leu-OMe.
Dutta, Anand S,Cormley, James J,McLachlan, Peter F,Major, John S
, p. 101 - 170 (2007/10/02)
A protected tetrapeptide derivative, Boc-D-Phe-Cys(Acm)-D-Trp-Leu-OMe (1) was found to inhibit human renin (IC50 4E-5M).Further structure activity relationship studies based on 1 showed that the N-t-butoxycarbonyl and the methyl ester groups and the leucine residue were not critical for the renin inhibitory activity.Compounds with similar or improved potency could be made by various modifications of these residues.The other three amino-acid residues were much more important for activity.All the D-Trp substituted analogues were inactive.The Cys(Acm) residue could only be replaced by amino acid residues containing a basic group in the side-chain.With the exception of D-α-MePhe all the other substitutions in the D-Phe position gave compounds less potent than 1.